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Q2M3T9 (HYAL4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase-4

Short name=Hyal-4
EC=3.2.1.35
Alternative name(s):
Chondroitin sulfate endo-beta-N-acetylgalactosaminidase
Chondroitin sulfate hydrolase
Short name=CSHY
Hyaluronoglucosaminidase-4
Gene names
Name:HYAL4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide. Ref.2 Ref.7

Catalytic activity

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Detected in placenta and skeletal muscle. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5-5 (for chondroitin sulfate hydrolase activity). Ref.2

Temperature dependence:

Optimum temperature is 37 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Hyaluronidase-4
PRO_0000301999

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 453424Extracellular Potential
Transmembrane454 – 47421Helical; Potential
Topological domain475 – 4817Cytoplasmic Potential

Sites

Active site1471Proton donor By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) (complex) Ref.8
Glycosylation3431N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 351 By similarity
Disulfide bond223 ↔ 237 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 435 By similarity
Disulfide bond437 ↔ 446 By similarity

Natural variations

Natural variant3461A → S. Ref.6
Corresponds to variant rs6949082 [ dbSNP | Ensembl ].
VAR_034936

Experimental info

Sequence conflict2631G → C in AAC98883. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2M3T9 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 9D530009AA898D1F

FASTA48154,249
        10         20         30         40         50         60 
MKVLSEGQLK LCVVQPVHLT SWLLIFFILK SISCLKPARL PIYQRKPFIA AWNAPTDQCL 

        70         80         90        100        110        120 
IKYNLRLNLK MFPVIGSPLA KARGQNVTIF YVNRLGYYPW YTSQGVPING GLPQNISLQV 

       130        140        150        160        170        180 
HLEKADQDIN YYIPAEDFSG LAVIDWEYWR PQWARNWNSK DVYRQKSRKL ISDMGKNVSA 

       190        200        210        220        230        240 
TDIEYLAKVT FEESAKAFMK ETIKLGIKSR PKGLWGYYLY PDCHNYNVYA PNYSGSCPED 

       250        260        270        280        290        300 
EVLRNNELSW LWNSSAALYP SIGVWKSLGD SENILRFSKF RVHESMRIST MTSHDYALPV 

       310        320        330        340        350        360 
FVYTRLGYRD EPLFFLSKQD LVSTIGESAA LGAAGIVIWG DMNLTASKAN CTKVKQFVSS 

       370        380        390        400        410        420 
DLGSYIANVT RAAEVCSLHL CRNNGRCIRK MWNAPSYLHL NPASYHIEAS EDGEFTVKGK 

       430        440        450        460        470        480 
ASDTDLAVMA DTFSCHCYQG YEGADCREIK TADGCSGVSP SPGSLMTLCL LLLASYRSIQ 


L 

« Hide

References

« Hide 'large scale' references
[1]"Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31."
Csoka A.B., Scherer S.W., Stern R.
Genomics 60:356-361(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Identification of human hyaluronidase-4 as a novel chondroitin sulfate hydrolase that preferentially cleaves the galactosaminidic linkage in the trisulfated tetrasaccharide sequence."
Kaneiwa T., Mizumoto S., Sugahara K., Yamada S.
Glycobiology 20:300-309(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-346.
Tissue: Cerebellum.
[7]"Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis."
Jedrzejas M.J., Stern R.
Proteins 61:227-238(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, 3D-STRUCTURE MODELING.
[8]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-177.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009010 mRNA. Translation: AAC98883.1.
AB470346 mRNA. Translation: BAI49593.1.
AC006029 Genomic DNA. Translation: AAD43186.1.
CH236947 Genomic DNA. Translation: EAL24331.1.
CH471070 Genomic DNA. Translation: EAW83603.1.
BC104788 mRNA. Translation: AAI04789.1.
BC104790 mRNA. Translation: AAI04791.1.
CCDSCCDS5789.1.
RefSeqNP_036401.2. NM_012269.2.
XP_005250295.1. XM_005250238.1.
UniGeneHs.28673.

3D structure databases

ProteinModelPortalQ2M3T9.
SMRQ2M3T9. Positions 48-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000223026.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

PTM databases

PhosphoSiteQ2M3T9.

Polymorphism databases

DMDM158564281.

Proteomic databases

PaxDbQ2M3T9.
PRIDEQ2M3T9.

Protocols and materials databases

DNASU23553.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223026; ENSP00000223026; ENSG00000106302.
ENST00000476325; ENSP00000417186; ENSG00000106302.
GeneID23553.
KEGGhsa:23553.
UCSCuc003vlc.3. human.

Organism-specific databases

CTD23553.
GeneCardsGC07P123469.
H-InvDBHIX0033519.
HGNCHGNC:5323. HYAL4.
HPAHPA029453.
MIM604510. gene.
neXtProtNX_Q2M3T9.
PharmGKBPA29574.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77606.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidQ2M3T9.
KOK01197.
OMAWNTKDVY.
PhylomeDBQ2M3T9.
TreeFamTF321598.

Enzyme and pathway databases

BioCycMetaCyc:HS02883-MONOMER.

Gene expression databases

ArrayExpressQ2M3T9.
BgeeQ2M3T9.
CleanExHS_HYAL4.
GenevestigatorQ2M3T9.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23553.
NextBio46112.
PROQ2M3T9.
SOURCESearch...

Entry information

Entry nameHYAL4_HUMAN
AccessionPrimary (citable) accession number: Q2M3T9
Secondary accession number(s): D0VXG1, Q9UL99, Q9Y6T9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries